Dataset Information
Cryo-EM structure of human lipid phosphate phosphatase 1
Ontology highlight
ABSTRACT:
SUBMITTER: Hongwu Qian
PROVIDER: EMPIAR-13186 | biostudies-other |
REPOSITORIES: biostudies-other
Publications
Structural basis for the catalytic mechanism of human lipid phosphate phosphatases.
Nature chemical biology 20260109 5
Lipid phosphate phosphatases (LPPs) catalyze the dephosphorylation of a broad range of bioactive lipid phosphates, including lysophosphatidic acid and sphingosine-1-phosphate, playing essential roles in embryonic vasculogenesis, cell differentiation and inflammation. Here we present the cryo-electron microscopic structure of human LPP1 as a tetramer with C4 symmetry. We capture the phosphohistidine intermediate state by using vanadate as a phosphate analog, where vanadate is coordinated by posit ...[more]